Critical role of tyrosine-20 in formation of gold nanoclusters within lysozyme: a molecular dynamics study

Ben A. Russell, Karina Kubiak-Ossowska, Yu Chen, Paul A. Mulheran

Research output: Contribution to journalArticle

Abstract

Lysozyme is one of the most commonly used proteins for encapsulating gold nanoclusters, yielding Ly-AuNC complexes. While possible applications of Ly-AuNCs in environmental, biological and trace metal sensing in solution have been demonstrated, there is currently a poor understanding of the physical characteristics of the Ly-AuNC complex. In this study we have employed fully atomistic molecular dynamics simulations to gain an understanding of the formation of Au clusters within the protein. It was found that in order to form AuNCs in the simulations, an approach of targeted insertion of Au atoms at a critical surface residue was needed. Tyrosine is known to be crucial for the reduction of Au salts experimentally, and our simulations showed that Tyr20 is the key residue for the formation of an AuNC beneath the protein surface in the α-helical domain. It is hoped these observations will aid future improvements and modification of Ly-AuNCs via alterations of the alpha-helix domain or Tyr20.
LanguageEnglish
Pages4907-4911
Number of pages5
JournalPhysical Chemistry Chemical Physics
Volume21
Issue number9
Early online date7 Feb 2019
DOIs
Publication statusPublished - 7 Mar 2019

Fingerprint

Nanoclusters
tyrosine
lysozyme
Muramidase
nanoclusters
Gold
Tyrosine
Molecular dynamics
gold
molecular dynamics
proteins
Membrane Proteins
Proteins
encapsulating
simulation
Salts
Atoms
helices
insertion
Computer simulation

Keywords

  • lysozyme
  • gold nanoclusters
  • metal sensing
  • molecular dynamic simulations

Cite this

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Critical role of tyrosine-20 in formation of gold nanoclusters within lysozyme : a molecular dynamics study. / Russell, Ben A.; Kubiak-Ossowska, Karina; Chen, Yu; Mulheran, Paul A.

In: Physical Chemistry Chemical Physics, Vol. 21, No. 9, 07.03.2019, p. 4907-4911.

Research output: Contribution to journalArticle

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T2 - Physical Chemistry Chemical Physics

AU - Russell, Ben A.

AU - Kubiak-Ossowska, Karina

AU - Chen, Yu

AU - Mulheran, Paul A.

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AB - Lysozyme is one of the most commonly used proteins for encapsulating gold nanoclusters, yielding Ly-AuNC complexes. While possible applications of Ly-AuNCs in environmental, biological and trace metal sensing in solution have been demonstrated, there is currently a poor understanding of the physical characteristics of the Ly-AuNC complex. In this study we have employed fully atomistic molecular dynamics simulations to gain an understanding of the formation of Au clusters within the protein. It was found that in order to form AuNCs in the simulations, an approach of targeted insertion of Au atoms at a critical surface residue was needed. Tyrosine is known to be crucial for the reduction of Au salts experimentally, and our simulations showed that Tyr20 is the key residue for the formation of an AuNC beneath the protein surface in the α-helical domain. It is hoped these observations will aid future improvements and modification of Ly-AuNCs via alterations of the alpha-helix domain or Tyr20.

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